Gene Ontology annotation based on Enzyme Commission mapping
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Automatic Gene Ontology annotation based on Rhea mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Mutations in the gene encoding 11-cis retinol dehydrogenase cause delayed dark adaptation and fundus albipunctatus.
-
RDH5 mutations cause fundus albipunctatus, a form of stationary night blindness with delayed regeneration of cone and rod photopigments; recombinant mutant enzymes had reduced activity relative to wild type. Establishes the visual-perception role of RDH5.
"Our results suggest that mutant alleles in RDH5 are a cause of fundus albipunctatus, a rare form of stationary night blindness characterized by a delay in the regeneration of cone and rod photopigments."
Biochemical defects in 11-cis-retinol dehydrogenase mutants associated with fundus albipunctatus.
-
RDH5 is a dimeric ER-membrane 11-cis-retinol dehydrogenase; 11 fundus-albipunctatus mutants showed decreased stability, mislocalization, and loss of enzymatic activity.
"All RDH5 mutants showed decreased protein stability and subcellular mislocalization and, in most cases, loss of enzymatic activity in vitro and in vivo."
Inhibition of dihydrotestosterone synthesis in prostate cancer by combined frontdoor and backdoor pathway blockade.
-
RDH5 is one of four 3-alpha-oxidoreductases that convert androsterone to 5-alpha-dione / 5-alpha-androstane-3-alpha,17-beta-diol to dihydrotestosterone; catalytic Y175/K179 residues are required for activity. Supports the androsterone dehydrogenase EXP annotation.
"metabolism of 5α-androstan-3α-ol-17-one (androsterone; AND) to 5α-dione"
Identification and characterization of a stereospecific human enzyme that catalyzes 9-cis-retinol oxidation. A possible role in 9-cis-retinoic acid formation.
-
The cloned enzyme (RDH5/9-cis-retinol dehydrogenase) avidly oxidizes 9-cis-retinol and, less efficiently, 13-cis-retinol, prefers NAD+, and does not catalyze all-trans-retinol oxidation. Directly refutes an all-trans-retinol dehydrogenase assignment.
"This protein also catalyzes oxidation of 13-cis-retinol at a rate approximately 10% of that of the 9-cis isomer but does not catalyze all-trans-retinol oxidation."
Activity of human 11-cis-retinol dehydrogenase (Rdh5) with steroids and retinoids and expression of its mRNA in extra-ocular human tissue.
-
Recombinant human RDH5 metabolizes 9-cis- and 11-cis-retinol with comparable efficiency and recognizes 5-alpha-androstane-3-alpha,17-beta-diol and androsterone as substrates (3-alpha-HSD activity) but not testosterone, DHT, oestradiol or corticosterone.
"recognizes 5alpha-androstan-3alpha,17beta-diol and androsterone as substrates (3alpha-hydroxysteroid dehydrogenase activity)"
The canonical retinoid cycle in rods (twilight vision)
RDH5 oxidises 11cROL to 11cRAL
Defective RDH5 does not oxidise 11cROL to 11cRAL and causes RPA
RDH5,RDH11 oxidise 11cROL to 11cRAL